Identification of a sulfate-bearing molecule associated with HLA class II antigens.

Abstract

The human Ia antigens (DR, DS, and SB), determined by genes contained within the HLA complex on chromosome 6, are glycoprotein heterodimers consisting of a Mr approximately equal to 34,000 alpha chain and a Mr approximately equal to 28,000 beta chain. As a result of studies exploring the possibility that alpha or beta (or both) might be sulfated, a unique component of the oligomeric Ia antigen complex was discovered. When anti-Ia immunoprecipitates from Nonidet P-40 lysates of [35S]sulfate-labeled lymphoid cells were analyzed by NaDodSO4/PAGE, a molecule of considerable size heterogeneity (Mr 40,000-70,000) was observed. This component was present in both anti-DR and anti-DS immunoprecipitates prepared from both human tonsil cells and lymphoblastoid B-cell lines but was not observed in control precipitates or in association with immunoglobulin or class I HLA molecules. Preliminary biochemical studies indicate that this Mr 40,000-70,000 molecule is polyanionic, disperse in molecular weight, and sensitive to protease digestion. The sulfate-bearing moiety of this component was resistant to Pronase but sensitive to chondroitinase ABC, indicating that this molecule belongs to the chondroitin sulfate class of proteoglycans.